Property-controlling Enzymes at the Membrane Interface

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Fältnamn	Indikatorer	Metadata
000		03871nam a2200421 4500
001		oai:DiVA.org:su-61988
003		SwePub
008		110906s2011 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
020		a 9789174473308q print
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-619882 URI
040		a (SwePub)su
041		a engb eng
042		9 SwePub
072	7	a vet2 swepub-contenttype
072	7	a dok2 swepub-publicationtype
100	1	a Ge, Changrong,d 1980-u Stockholms universitet,Institutionen för biokemi och biofysik,Åke Wieslander4 aut0 (Swepub:su)chge7872
245	1 0	a Property-controlling Enzymes at the Membrane Interface
264	1	a Stockholm :b Department of Biochemistry and Biophysics, Stockholm University,c 2011
300		a 80 s.
338		a electronic2 rdacarrier
500		a At the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 3: Manuscript. Paper 5: Manuscript.
520		a Monotopic proteins represent a specialized group of membrane proteins in that they are engaged in biochemical events taking place at the membrane interface. In particular, the monotopic lipid-synthesizing enzymes are able to synthesize amphiphilic lipid products by catalyzing two biochemically distinct molecules (substrates) at the membrane interface. Thus, from an evolutionary point of view, anchoring into the membrane interface enables monotopic enzymes to confer sensitivity to a changing environment by regulating their activities in the lipid biosynthetic pathways in order to maintain a certain membrane homeostasis. We are focused on a plant lipid-synthesizing enzyme DGD2 involved in phosphate shortage stress, and analyzed the potentially important lipid anchoring segments of it, by a set of biochemical and biophysical approaches. A mechanism was proposed to explain how DGD2 adjusts its activity to maintain a proper membrane. In addition, a multivariate-based bioinformatics approach was used to predict the lipid-binding segments for GT-B fold monotopic enzymes. In contrast, a soluble protein Myr1 from yeast, implicated in vesicular traffic, was also proposed to be a membrane stress sensor as it is able to exert different binding properties to stressed membranes, which is probably due to the presence of strongly plus-charged clusters in the protein. Moreover, a bacterial monotopic enzyme MGS was found to be able to induce massive amounts of intracellular vesicles in Escherichia coli cells. The mechanisms involve several steps: binding, bilayer lateral expansion, stimulation of lipid synthesis, and membrane bending. Proteolytic and mutant studies indicate that plus-charged residues and the scaffold-like structure of MGS are crucial for the vesiculation process. Hence, a number of features are involved governing the behaviour of monotopic membrane proteins at the lipid bilayer interface.
650	7	a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650	7	a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653		a monotopic membrane protein
653		a lipid-protein interaction
653		a membrane curvature
653		a glycosyltransferase
653		a Rossmann fold
653		a Biochemistry
653		a Biokemi
653		a biokemi
653		a Biochemistry
700	1	a Wieslander, Åke,c Professoru Stockholms universitet,Institutionen för biokemi och biofysik4 ths
700	1	a Guerin, Marcelo E.,c Ikerbasque Research Professoru University of the Basque Country4 opn
710	2	a Stockholms universitetb Institutionen för biokemi och biofysik4 org
856	4	u https://su.diva-portal.org/smash/get/diva2:439223/FULLTEXT01.pdfx primaryx Raw objecty fulltext
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-61988

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